Description
Key facts
Cell type:A549,
Species or organism:Human,
Tissue:Lung,
Knockout validation:Sanger Sequencing,Western blot,
Mutation description:Knockout achieved by using CRISPR/Cas9, 11 bp deletion in exon1 and 1 bp insertion in exon1.,
Disease:Carcinoma
Product details:
Knockout cell lysate achieved by CRISPR/Cas9.
REACH authorisation
Abcam has not and does not intend to apply for the REACH Authorisation of customers' uses of products that contain European Authorisation list (Annex XIV) substances.
It is the responsibility of our customers to check the necessity of application of REACH Authorisation, and any other relevant authorisations, for their intended uses.
Lysate preparation:
Our lysates are made using RIPA buffer to which we add a protease inhibitor cocktail and phosphatase inhibitor cocktail (ratio: 300:100:10).
This means that the protein of interest is denatured.
If you require a native form of the protein please use the live cell version. Please refer to our lysis protocol for further details on how our lysates are prepared.
User storage instructions:
Lyophilizate may be stored at 4°C. After reconstitution, store at -20°C for short-term storage or -80°C for long-term storage.
This product is subject to limited use licenses from The Broad Institute, ERS Genomics Limited and Sigma-Aldrich Co. LLC, and is developed with patented technology. For full details of the licenses and patents please refer to our
limited use license
patent pages
Properties and Storage Information:
Gene name-PML, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Western blot, Shipped at conditions-Ambient - Can Ship with Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
The PML protein also known as promyelocytic leukemia protein has a mass of about 97 kilodaltons. PML is typically expressed in the nucleus in distinct structures called nuclear bodies. These nuclear bodies often referred to as PML-nuclear bodies or PML-NBs serve several functions within the cell. The PML protein is commonly identified in tissues such as the bone marrow and blood cells where it plays a significant role in various cellular processes. Numerous antibodies including anti-PML are used to study the distribution and function of PML protein in different cellular contexts.
Biological function summary
The PML protein interacts with various molecular partners and forms a part of multiprotein complexes within the PML-nuclear bodies. Its functions include the regulation of transcription induction of apoptosis DNA damage response and control of cell proliferation. PML can recruit other proteins such as p53 a tumor suppressor protein to influence these cellular activities. PML's ability to act as a scaffold within these complexes makes it essential for maintaining cellular homeostasis and response to stress. Various techniques such as PML protein ELISA are used to analyze PML-related biological activities.
Pathways
The PML protein plays a significant role in critical cellular pathways such as apoptosis and the interferon response pathway. PML's interaction with the p53 protein links it to the apoptosis pathway where it acts as an inducer of cell death in response to cellular stress and damage. In the interferon response pathway PML contributes to antiviral defense mechanisms. The involvement of PML in these pathways emphasizes its importance in cellular defense and programmed cell death. Related proteins like STATs (signal transducers and activators of transcription) are known to interact with PML in these pathways.
Abnormalities in PML protein expression and function are linked to specific diseases including acute promyelocytic leukemia (APL) and certain types of cancer. Acute promyelocytic leukemia is characterized by a translocation involving the PML gene resulting in the PML-RARα fusion protein which interferes with normal cell differentiation. PML also relates to neurodegenerative disorders where changes in PML expression impact cellular stress responses. In the context of these diseases the PML protein's interaction with oncogenic proteins like RARα in leukemia highlights its role in disease development and potential as a therapeutic target.
